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Literature summary for 2.8.1.7 extracted from

  • Mihara, H.; Fujii, T.; Kato, S.; Kurihara, T.; Hata, Y.; Esaki, N.
    Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine (2002), J. Biochem., 131, 679-685.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, complexed with L-propargylglycine Escherichia coli

Protein Variants

Protein Variants Comment Organism
H123A decreased specific activity towards L-selenocysteine Escherichia coli
H55A normal activity towards L-selenocysteine and L-cysteine Escherichia coli
R379A significant loss of activity towards L-selenocysteine Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-cysteine + [enzyme]-cysteine Escherichia coli
-
 L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.05
-
 H123 mutant with L-selenocysteine as substrate Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + [enzyme]-cysteine
-
 Escherichia coli L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
L-cysteine + [enzyme]-cysteine Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine Escherichia coli L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
L-selenocysteine Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine Escherichia coli L-alanine + selenium
-
 ?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Escherichia coli